3.4.24.B26: myroilysin
This is an abbreviated version!
For detailed information about myroilysin, go to the full flat file.
Word Map on EC 3.4.24.B26
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3.4.24.B26
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myroides
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metalloproteases
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profundi
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deep-sea
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astacin
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medicine
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synthesis
- 3.4.24.B26
-
myroides
- metalloproteases
- profundi
-
deep-sea
- astacin
- medicine
- synthesis
Reaction
broad specificity, elastinolytic activity and collagen-swelling ability =
Synonyms
M10.064, More, MPR_2201
ECTree
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Crystallization
Crystallization on EC 3.4.24.B26 - myroilysin
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crystal structures of pro-myroilysin. The catalytic zinc ion of pro-myroilysin, at the bottom of a deep active site, is coordinated by three histidine residues in the conserved motif HEXXHXXGXXH. The cysteine residue in the propeptide coordinates the catalytic zinc ion and inhibits myroilysin activity. A cap structure tops the active site cleft in the structure of pro-myroilysin